Immunological study of anthranilate synthetase.
AUTOR(ES)
Reiners, J J
RESUMO
An immunological study of anthranilate synthetase (ASase) has been initiated using quantitative precipitation, enzyme neutralization, and immunodiffusion methods. Cross-reactivity of anthranilate synthetase-anthranilate-5-phosphoribosylpyrophosphate phosphoribosyltransferase (ASase-PRTase) from Escherichia coli, Klebsiella aerogenes, and Salmonella typhimurium and ASase from Serratia marcescens and Pseudomonas putida was detected with antibodies to ?E. coli trypsin-treated ASase. Cross-reactivity of antigens was also obtained with S. marcescens anti-ASase. Indices of dissimilarity verified the overall structural similarity of ASase-PRTase from E. coli, K. aerogenes, and S. typhimurium and the divergence from S. marcescens ASase. Further divergence of these enzymes from ASase in B. subtilis and P. putida was apparent. Precipitation of ASase components I and II (ASase CoI and ASase CoII) was obtained using anti-ASase or antiserum fractionated to contain component-specific antibodies. Anti-ASase inhibited enzyme activity to binding to determinants on both subunits. Anti-ASase CoI inhibited the ammonia-dependent reaction and interfered with amide transfer from glutaminyl-ASase CoII. Anti-ASase CoII inhibited the glutamine reaction by blocking amide transfer. Enzyme neutralization experiments indicate more conservation of determinants at the active site region of ASase CoII compared to ASase CoI in the enterobacteria. A particulate form of ASase-PRTase in E. coli, K. aerogenes, and S. typhimurium could be distinguished by quantitative precipitation and immunodiffusion.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=235768Documentos Relacionados
- Nucleotide sequence of Escherichia coli pabB indicates a common evolutionary origin of p-aminobenzoate synthetase and anthranilate synthetase.
- Immunological crossreactivity of eukaryotic C1-tetrahydrofolate synthase and prokaryotic 10-formyltetrahydrofolate synthetase.
- Biosynthesis of bacterial glycogen: purification and structural and immunological properties of Rhodopseudomonas sphaeroides ADPglucose synthetase.
- Regulation of glutamine synthetase. 8. ATP: glutamine synthetase adenylyltransferase, an enzyme that catalyzes alterations in the regulatory properties of glutamine synthetase.
- Regulation of synthesis of glutamine synthetase by adenylylated glutamine synthetase.
